Abstract
In this paper we report dielectric measurements at radiofrequencies on aqueous solutions of three proteins (cytochrome, lysozyme and metmyoglobin) in the native state as a function of temperature in the interval 0–60°C. From the analysis of dielectric relaxation of the protein solutions, the effective hydrodynamic radius r and the electric dipole moment μ of the proteins were calculated. The results show that temperature causes continuous gradual changes of r and μ, with a maximum at a temperature that is different for each protein. This effect in the pre-melting region seems to be general and related to variations of thermodynamic parameters.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
